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J. Biol. Chem., Vol. 280, Issue 52, 43073-43078, December 30, 2005

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The Crystal Structure of the Bacillus anthracis Spore Surface Protein BclA Shows Remarkable Similarity to Mammalian Proteins^*

Stéphane Réty, Sylvie Salamitou, Ignacio Garcia-Verdugo¶, David J. S. Hulmes||, Françoise Le Hégarat, Richard Chaby¶, and Anita Lewit-Bentley1

From the Laboratoire de Biotechnologies et Pharmacologie Génétique Appliquées, CNRS, Unité Mixte de Recherche 8113, Ecole Normale Supérieure de Cachan, 61 Avenue du Président Wilson, 94235 Cachan, France, Institut de Génétique et Microbiologie, CNRS, Unité Mixte de Recherche 8621, Bât. 409, Université Paris XI, 91405 Orsay, France, ^¶Equipe "Endotoxines", Institut de Biochimie et de Biophysique Moléculaire et Cellulaire, CNRS, Unité Mixte de Recherche 8619, Bât. 430, Université Paris XI, 91405 Orsay, France, and ^||Institut de Biologie et Chimie des Protéines, CNRS Unité Mixte de Recherche 5086, 7 Passage du Vercors, 69367 Lyon cedex 7, France

The lethal disease anthrax is propagated by spores of Bacillus anthracis, which can penetrate into the mammalian host by inhalation, causing a rapid progression of the disease and a mostly fatal outcome. We have solved the three-dimensional structure of the major surface protein BclA on B. anthracis spores. Surprisingly, the structure resembles C1q, the first component of complement, despite there being no sequence homology. Although most assays for C1q-like activity, including binding to C1q receptors, suggest that BclA does not mimic C1q, we show that BclA, as well as C1q, interacts with components of the lung alveolar surfactant layer. Thus, to better recognize and invade its hosts, this pathogenic soil bacterium may have evolved a surface protein whose structure is strikingly close to a mammalian protein.

Received for publication, September 14, 2005

The atomic coordinates and structure factors (code 1wck) have been deposited in the Protein Data Bank, Research Collaboratory for Structural Bioinformatics, Rutgers University, New Brunswick, NJ (http://www.rcsb.org/).

^* This work was supported in part by the Fondation pour la Recherche Médicale. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The on-line version of this article (available at http://www.jbc.org) contains supplemental Fig. 1.

¹ To whom correspondence should be addressed. Tel.: 33-1-47-40-76-65; Fax: 33-1-47-40-76-71; E-mail: anita.bentley{at}lbpa.ens-cachan.fr.

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